(Q47334829)

14 January 2018

title

Real time kinetics of the DnaK/DnaJ/GrpE molecular chaperone machine action. (English)

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14 January 2018

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2

Zylicz M

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14 January 2018

Banecki B

1

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14 January 2018

language of work or name

English

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publication date

1 March 1996

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14 January 2018

Journal of Biological Chemistry

published in

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14 January 2018

volume

271

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page(s)

6137-6143

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issue

11

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14 January 2018

A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

The general concept of molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Specificity of DnaK-peptide binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

An enzyme that removes clathrin coats: purification of an uncoating ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Eukaryotic DnaJ homologs and the specificity of Hsp70 activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

Calf thymus Hsc70 protein protects and reactivates prokaryotic and eukaryotic enzymes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.11.6137

21 January 2018

Identifiers

DOI

10.1074/JBC.271.11.6137

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14 January 2018

PubMed ID

8626401

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14 January 2018